Crystal structure of 14-3-3 sigma in complex with Tau pS214 peptide and covalent stabilizer AO184. Determined by X-ray diffraction at 1.45 Å resolution. Released 9 Jul 2025.
Explore 9FVG in 3D Show helices and sheets RCSB PDB PDBe
9FVG contains 14 α-helices and 0 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-15 | 13 | |
| α-helix | 19-31 | 13 | |
| α-helix | 35-37 | 3 | |
| α-helix | 38-69 | 32 | |
| α-helix | 80-102 | 23 | |
| α-helix | 103-107 | 5 | |
| α-helix | 108-110 | 3 | |
| α-helix | 114-134 | 21 | |
| α-helix | 140-161 | 22 | |
| α-helix | 167-178 | 12 | |
| α-helix | 179-183 | 5 | |
| α-helix | 187-204 | 18 | |
| α-helix | 205-207 | 3 | |
| α-helix | 210-230 | 21 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 14-3-3 protein sigma | A | protein | 236 | Homo sapiens | P31947 (AlphaFold model) |
| Microtubule-associated protein tau | P | protein | 13 | Homo sapiens | P10636 (AlphaFold model) |
>9FVG_1 14-3-3 protein sigma (chains A) GAMGSMERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQ RAAWRVLSSIEQKSNEEGSEEKGPEVREYREKVETELQGVCDTVLGLLDSHLIKEAGDAE SRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAMDISKKEMPPTNPIRLGLALN FSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWT
>9FVG_2 Microtubule-associated protein tau (chains P) SRTPSLPTPPTRE
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1IF3 | 1-(3-bromanyl-4-methyl-phenyl)-2-(4-ethylphenyl)imidazole | C18 H17 Br N2 | 1 |
Site-selective stabilization of the 14-3-3/tau protein-protein interaction. Oberheide, A.O., van den Oetelaar, M.C.M., Scheele, J.J.A. et al. To be published.
Other PDB entries of the same protein (UniProt P31947 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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